DOCSLIB.ORG

High Performance Liquid Chromatography Method for the Determination of Pyridoxal-5-Phosphate in Human Plasma

Total Page：16

File Type：pdf, Size：1020Kb

Download full-text PDF Read full-text
High Performance Liquid Chromatography Method for the Determination of Pyridoxal-5-Phosphate in Human Plasma European Journal of Clinical Nutrition (1999) 53, 448±455 ß 1999 Stockton Press. All rights reserved 0954±3007/99 $12.00 http://www.stockton-press.co.uk/ejcn High performance liquid chromatography method for the determination of pyridoxal-5-phosphate in human plasma: How appropriate are cut-off values for vitamin B6 de®ciency? AL Bailey1*, AJA Wright1 and S Southon1 1Nutrition, Diet and Health Department, Institute of Food Research, Norwich Research Park, NR4 7UA, UK. Objectives: Application of a HPLC (high performance liquid chromatography) method, using cyanide derivatisation, to the determination of plasma pyridoxal-5-phosphate (PLP) concentrations as an indicator of vitamin B6 adequacy. Setting: The study was performed at the Institute of Food Research, Norwich, UK. Blood samples were taken at the Institute, at Health Centres, or in the volunteer's home. Subjects: 51 adolescent, 131 adult, 68 non-institutionalized elderly and 44 aged (>73 y) volunteers were recruited from local authority schools, local Health Centres and General Practitioners. Results: The mean PLP recovery was 92.8%. The intra- and inter-assay coef®cients of variation were 2.8% and 5.2% respectively. Mean PLP concentrations for males and females, respectively, were: adolescents (13 ± 14 y), 36.4 and 43.5 nM; adults (20 ± 64 y), 39.2 and 40.0 nM; elderly (68 ± 73 y), 34.8 and 35.3 nM; aged (>73 y), 57.8 and 49.0 nM. Percentages of subjects with PLP concentrations < 34.4 nM were over 26% in all population groups. Mean vitamin B6 intakes (mg=g protein intake), as assessed by weighed dietary records, were all above reference nutrient intakes (15 mg=g protein). Conclusions: An HPLC method, using cyanide derivitisation, has been applied to the determination of plasma PLP. Comparisons of results for local population groups with current cut-off values for plasma PLP, show large numbers of volunteers at risk of vitamin B6 de®ciency although this is not re¯ected by vitamin B6 intakes calculated from food tables. The 34.4 nM cut-off value for value for plasma PLP, indicating de®ciency, is questioned. Sponsorship: UK Ministry of Agriculture, Fisheries and Food; Department of Education and Science; Vitamin Forum. Descriptors: Vitamin B6; Plasma pyridoxal-5-phosphate; HPLC; Cyanide derivative Introduction The total body pool of vitamin B6 is around 200 mg (Coburn et al, 1988) (Note: not 20 ± 30 mg as quoted by Vitamin B (active 3-hydroxy-2-methylpyridine deriva- 6 Gibson, 1990). About 70 ± 80% of this pool is in skeletal tives) is an essential precursor for the pyridoxal-5-phos- muscle and is resistant to depletion, reducing only after 6 phate (PLP) coenzyme for protein and, to a lesser extent, weeks of low intake (1.76 mmol=d; 0.37 mg=d pyridoxine carbohydrate and lipid metabolism. More recently a range hydrochloride) in adult males (Coburn et al, 1991). How- of additional roles have been suggested for this vitamin: (i) ever, the major transport form of vitamin B is PLP, which prevention of atherosclerorosis (Murray & Pizzorno, 6 declines relatively rapidly at low dietary intake. Thus, 1990a; Vermaak et al, 1987; Ubbink, 1994; Verhoef & measurement of this active coenzyme form of vitamin B Stampfer, 1995; Selhub et al, 1993); (ii) optimization of 6 in plasma is more likely to re¯ect short-term intake than immune function (Rall & Meydani, 1993); (iii) treatment of muscle B which is tightly bound to glycogen phosphoryl- premenstrual tension (PMT) (Murray & Pizzorno, 1990b; 6 ase and only turns over as this enzyme does (Coburn et al, Kleijnen, et al, 1991); (iv) prevention of nausea and 1991). Low plasma concentrations of PLP, therefore, do not vomiting during pregnancy (Vir et al, 1980; Guilarte, re¯ect muscle concentration but may provide a good 1993; (v) learning and memory (Guilarte, 1993; Kleijnen indication of de®ciency risk. & Knipschild, 1991); (vi) alteration of steroid hormone Biochemical methods, developed over the last twenty responsiveness, and thus, the aetiology and treatment of years for the determination of PLP concentrations in certain cancers and hypertension (Bender, 1994); (vii) biological samples, include microbiological, spectrophoto- treatment of psychiatric patients (Sandyk & Pardeshi, metric, ¯uorometric, enzymatic, radio-enzymatic, and chro- 1990; Bender, 1992; Stewart et al, 1984). matography (Sauberlich, 1984, Vanderslice et al, 1985; Leklem, 1990). No single method has been recommended for determination of vitamin B6 adequacy (Leklem, 1990; *Correspondence (and guarantor): AL Bailey, Nutrition, Diet and Health Li & Lumeng, 1980; Bender, 1993). Department, Institute of Food Research, Norwich Research Park, NR4 Separation of PLP from other B vitamins is easily 7UA, UK. 6 Received 7 November 1998; revised 14 January 1999; accepted 16 January achieved by high performance liquid chromatography 1999. (HPLC), but detection has to be achieved by formation of Plasma PLP by HPLC AL Bailey et al 449 UV absorbing, ¯uorescent or electrochemically active deri- 64 y, n 131, 64 males, 67 females) were recruited by vatives, since PLP has only low intrinsic ¯uorescence. The written invitation, at random from the General Practi- dif®culty with HPLC methods for the determination of tioners' lists of two local Health Centres (Norwich and plasma PLP has been their lack of sensitivity, since Dereham). Non-institutionalized elderly volunteers (68 ± 73 plasma PLP concentrations are typically in the 5 ± years, n 68 29 males, 39 females) and aged volunteers 100 ng=ml (20.3 ± 405 nM) range, necessitating relatively (74 ± 90 y, n 44, 15 males, 29 females) were randomly large sample sizes (0.3 ± 1.0 ml) (Sauberlich, 1984). selected from the age=gender registers of two General The use of cyanide to produce a highly ¯uorescent Practitioners in Norwich and recruited by written invita- derivative of PLP was ®rst used in 1959 (Ohishi & tion. Recruitment methods are described in full detail by Fukui, 1968, Adams, 1969, Tamura & Takanaski, 1970) Wright et al, (1995). and enabled more sensitivity than other derivatives. Cya- nide derivatisation of PLP was used in combination with HPLC in methods by Naoi et al (1988), who determined Sample preparation PLP concentrations in puri®ed enzymes, human brain Fresh, fasting (12 h) venous, whole blood was removed by homogenates and tissue cultured cells, but not human venepuncture into heparinized plastic tubes (Sarstedt, Lei- plasma. cester, UK), centrifuged (5006g,4C, 10 min) and 500 ml In the present paper, a method based on that of Naoi et of plasma removed into 2 ml plastic microfuge tubes al (1988) was used to measure PLP concentrations in small (Sarstedt, Leicester, UK) which were stored at 40 C (100 ml) volumes of plasma. This method facilitates studies until analysis. where small samples may be important, for example studies involving very young volunteers, or when a single sample Derivatisation needs to be used for a variety of biochemical assays. Minor Derivatisation of samples was performed under non-UV modi®cations to the method are described and reproduci- lighting. Duplicate aliquots (100 ml) of thawed plasma were bility and recovery data are presented, together with ranges pipetted into further microfuge tubes containing aqueous of PLP concentrations found in human adolscent adult, potassium phosphate buffer (100 ml, 10 mM; pH 7.4) and elderly and aged population groups. The incidence of deproteinized by the addition of trichloroacetic acid (TCA; vitamin B6 de®ciency, as judged by currently used cut-off 200 ml, 10% w=v). The samples were capped and heated for value for plasma PLP, was determined. How appropriate 15 min at 50C. After cooling to room temperature (20 ± these cut-off values are, as indicators of de®ciency, is 25C), dipotassium phosphate (140 ml, 3.3 M; pH 10.2) and considered. potassium cyanide (40 ml, 8 mM) were added, mixing tube contents after each addition. The cyanide derivatives of Materials and methods PLP and PA were formed by heating again at 50C for 25 min. After again cooling to room temperature the Reagents ¯uorescent derivatives were stabilized by addition of phos- All reagents were analytical grade unless speci®ed other- phoric acid (50 ml, 28%). Samples were centrifuged at wise. Pyridoxal-5-phosphate (PLP) and 4-pyridoxic acid 88006g for 5 min and the supernatants transferred to (PA) were obtained from Sigma Chemical Co, Dorset, UK. amber, crimp cap, auto sampler vials for HPLC analysis. All water was double glass distilled. Potassium cyanide was obtained from Sigma Chemical Co. (Dorset, UK). Pyridox- ine (PN), Pyridoxal (PL), pyridoxamine (PM) and pyridox- Chromatographic conditions amine-5-phosphate were also obtained from Sigma The analytical HPLC column was an ApexTM 3 mm ODS Chemical Company. (C18) I, 2560.4 cm id. (Jones Chromatography, Mid Gla- morgan, UK) instead of that used by Naoi et al (1988), Pyridoxal-5-phosphate and 4-pyridoxic acid standards (STRTM ODS-H; 150 mm64 mm id; 5 mm particle size; A stock PLP solution (50 mg=ml; 202.3 mM in 10 mM 100 AÊ pore size). Samples (50 ml) were injected by loop potassium phosphate buffer, pH 7.4) was prepared freshly ®lling using a RheodyneTM 7125 valve (Anachem, Luton, each week and stored at 4C in the dark. Working Bedfordshire, UK). The analytical column was protected by standard solutions were prepared daily by dilution of the use of a guard column packed with 40 mm C18 material stock 25 mg=l (0.1 mM) in 10 mM phosphate buffer. 2cm62 mm id, Anachem, Luton, UK). The HPLC pump For the additional determination of pyridoxic acid (PA), used was isocratic (SA 6410B, Severn Analytical, Hitchin a stock solution of PA (100 mg=l; 0.546 mM) was prepared Beds, UK). The mobile phase was 1 mM heptane sulphonic in 10 mM phosphate buffer and diluted together with PLP acid in 2 M potassium acetate, adjusted to pH 3.75 with to give a mixed PLP and PA standard (25 mg=l PLP and potassium hydroxide (solid).
Load more

Recommended publications
  • Pyridoxal Phosphate Is Better Than Pyridoxine for Controlling Idiopathic Intractable Epilepsy
    512 ORIGINAL ARTICLE Arch Dis Child: first published as 10.1136/adc.2003.045963 on 25 April 2005. Downloaded from Pyridoxal phosphate is better than pyridoxine for controlling idiopathic intractable epilepsy H-S Wang, M-F Kuo, M-L Chou, P-C Hung, K-L Lin, M-Y Hsieh, M-Y Chang ............................................................................................................................... Arch Dis Child 2005;90:512–515. doi: 10.1136/adc.2003.045963 Aim: To study the difference between pyridoxine (PN) and its active form, pyridoxal phosphate, (PLP) in control of idiopathic intractable epilepsy in children. Methods: Among 574 children with active epilepsy, 94 (aged 8 months to 15 years) were diagnosed with idiopathic intractable epilepsy for more than six months. All received intravenous PLP 10 mg/kg, then 10 mg/kg/day in four divided doses. If seizures recurred within 24 hours, another dose of 40 mg/kg was See end of article for given, followed by 50 mg/kg/day in four divided doses. For those patients whose seizures were totally authors’ affiliations controlled, PLP was replaced by the same dose of oral PN. If the seizure recurred, intravenous PLP was ....................... infused followed by oral PLP 50 mg/kg/day. Correspondence to: Results: Fifty seven patients had generalised seizures (of whom 13 had infantile spasms) and 37 had focal Dr M-F Kuo, Division of seizure. Eleven had dramatic and sustained responses to PLP; of these, five also responded to PN. Within (Pediatric) Neurosurgery, six months of treatment with PLP or PN, five of the 11 patients were seizure free and had their previous Department of Surgery, National Taiwan University antiepileptic medicine tapered off gradually.
    [Show full text]
  • Composition: Each
    ______________________________________________________________________________________________________________ Composition: Each Tablet Contains L-Methylfolate 1mg Mecobalamin 1500 mcg Pyridoxal 5’-phosphate 0.5mg Pharmacokinetic properties: L-methylfolate is a water soluble molecule which is primarily excreted via the kidneys. In a study of subjects with coronary artery disease (n=21), peak plasma levels were reached in 1-3 hours following ORAL/PARENTERAL administration. Peak concentrations of L-methylfolate were found to be more than seven times higher than folic acid (129 ng ml-1 vs. 14.1 ng ml-1) following ORAL/PARENTERAL administration. The mean elimination half-life is approximately 3 hours after 5mg of oral L- methylfolate, administered daily for 7 days. The mean values for Cmax, Tmax, and AUC0-12 were 129 ng ml-1, 1.3 hr., and 383 respectively. Red blood cells (RBCs) appear to be the storage depot for folate, as RBC levels remain elevated for periods in excess of 40 days following discontinuation of supplementation. Plasma protein binding studies showed that L-methylfolate is 56% bound to plasma proteins. Mecobalamin substances bind to intrinsic factor; a glycoprotein secreted by the gastric mucosa, and are then actively absorbed from the gastrointestinal tract. Absorption is impaired in patients with an absence of intrinsic factor, with a malabsorption syndrome or with disease or abnormality of the gut, or after gastrectomy. Absorption from the gastrointestinal tract can also occur by passive diffusion; little of the vitamin present in food is absorbed in this manner although the process becomes increasingly important with larger amounts such as those used therapeutically. After intranasal dosage, peak plasma concentrations of cyanocobalamin have been reached in 1 to 2 hours.
    [Show full text]
  • Vitamin B6 Metabolism and Regulation of Pyridoxal Kinase
    Virginia Commonwealth University VCU Scholars Compass Theses and Dissertations Graduate School 2009 VITAMIN B6 METABOLISM AND REGULATION OF PYRIDOXAL KINASE Amit Gandhi Virginia Commonwealth University Follow this and additional works at: https://scholarscompass.vcu.edu/etd Part of the Chemicals and Drugs Commons © The Author Downloaded from https://scholarscompass.vcu.edu/etd/2008 This Dissertation is brought to you for free and open access by the Graduate School at VCU Scholars Compass. It has been accepted for inclusion in Theses and Dissertations by an authorized administrator of VCU Scholars Compass. For more information, please contact [email protected]. © Amit K. Gandhi 2009 All Rights Reserved VITAMIN B 6 METABOLISM AND REGULATION OF PYRIDOXAL KINASE A dissertation submitted in partial fulfillment of the requirements for the degree of Doctor of Philosophy at Virginia Commonwealth University. By AMIT K. GANDHI M.S (Pharmaceutical Science), Rajiv Gandhi University, Indore, India, 2003 B.Pharm, Rajiv Gandhi University, Indore, India, 2001 Director: Martin K. Safo, Ph.D Assistant Professor, Department of Medicinal Chemistry Virginia Commonwealth University Richmond, Virginia December, 2009 Acknowledgement I would like to take this opportunity to express my deep gratitude and profound respect to my advisor, Dr. Martin K. Safo, for his supervision, advice, and guidance in this research work. His support and insight have been invaluable in the progression of my research. I also appreciate his words of encouragement, which kept me always in an innovative mood and guided me at all the times to bring about the best in me. He is my mentor and teacher whom I shall remember forever.
    [Show full text]
  • Phosphate-Dependent Enzymes Involved in Biotin Biosynthesis: Structure, Reaction Mechanism and Inhibition☆
    Biochimica et Biophysica Acta 1814 (2011) 1459–1466 Contents lists available at ScienceDirect Biochimica et Biophysica Acta journal homepage: www.elsevier.com/locate/bbapap Review Pyridoxal-5′-phosphate-dependent enzymes involved in biotin biosynthesis: Structure, reaction mechanism and inhibition☆ Stéphane Mann, Olivier Ploux ⁎ Laboratoire Charles Friedel, ENSCP Chimie ParisTech, UMR CNRS 7223, 11 rue Pierre et Marie Curie, F-75231 Paris Cedex 05, France article info abstract Article history: The four last steps of biotin biosynthesis, starting from pimeloyl-CoA, are conserved among all the Received 5 July 2010 biotin-producing microorganisms. Two enzymes of this pathway, the 8-amino-7-oxononanoate synthase Received in revised form 4 November 2010 (AONS) and the 7,8-diaminopelargonic acid aminotransferase (DAPA AT) are dependent on pyridoxal-5′- Accepted 10 December 2010 phosphate (PLP). This review summarizes our current understanding of the structure, reaction mechanism Available online 21 December 2010 and inhibition on these two interesting enzymes. Mechanistic studies as well as the determination of the crystal structure of AONS have revealed a complex mechanism involving an acylation with inversion of Keywords: fi fi 8-amino-7-oxononanoate synthase con guration and a decarboxylation with retention of con guration. This reaction mechanism is shared by the 7,8-diaminopelargonic acid aminotransferase homologous 5-aminolevulinate synthase and serine palmitoyltransferase. While the reaction catalyzed by Pyridoxal-5′-phosphate DAPA AT is a classical PLP-dependent transamination, the inactivation of this enzyme by amiclenomycin, a Enzyme reaction mechanism natural antibiotic that is active against Mycobacterium tuberculosis, involves the irreversible formation of an Inhibition adduct between PLP and amiclenomycin.
    [Show full text]
  • Large-Scale Domain Motions and Pyridoxal-5'-Phosphate Assisted Radical Catalysis in Coenzyme † B12-Dependent Aminomutases
    Int. J. Mol. Sci. 2014, 15, 3064-3087; doi:10.3390/ijms15023064 OPEN ACCESS International Journal of Molecular Sciences ISSN 1422-0067 www.mdpi.com/journal/ijms Review Large-Scale Domain Motions and Pyridoxal-5'-Phosphate Assisted Radical Catalysis in Coenzyme † B12-Dependent Aminomutases Amarendra Nath Maity, Yung-Han Chen and Shyue-Chu Ke * Physics Department, National Dong Hwa University, Hualien 97401, Taiwan; E-Mails: [email protected] (A.N.M.); [email protected] (Y.-H.C.) † This paper is dedicated to Emeritus Professor Perry A. Frey (Biochemistry Department, University of Wisconsin at Madison, Madison, WI, USA) on the occasion of his 78th birthday. * Author to whom correspondence should be addressed; E-Mail: [email protected]; Tel.: +886-3863-3705; Fax: +886-3863-3690. Received: 27 November 2013; in revised form: 25 December 2013 / Accepted: 22 January 2014 / Published: 20 February 2014 Abstract: Lysine 5,6-aminomutase (5,6-LAM) and ornithine 4,5-aminomutase (4,5-OAM) are two of the rare enzymes that use assistance of two vitamins as cofactors. These enzymes employ radical generating capability of coenzyme B12 (5'-deoxyadenosylcobalamin, dAdoCbl) and ability of pyridoxal-5'-phosphate (PLP, vitamin B6) to stabilize high-energy intermediates for performing challenging 1,2-amino rearrangements between adjacent carbons. A large-scale domain movement is required for interconversion between the catalytically inactive open form and the catalytically active closed form. In spite of all the similarities, these enzymes differ in substrate specificities. 4,5-OAM is highly specific for D-ornithine as a substrate while 5,6-LAM can accept D-lysine and L-β-lysine.
    [Show full text]
  • Prediagnostic Plasma Pyridoxal 5 -Phosphate (Vitamin B6) Levels
    Published OnlineFirst August 9, 2012; DOI: 10.1158/1055-9965.EPI-12-0717-T Cancer Epidemiology, Research Article Biomarkers & Prevention Prediagnostic Plasma Pyridoxal 50-Phosphate (Vitamin B6) Levels and Invasive Breast Carcinoma Risk: The Multiethnic Cohort Galina Lurie1, Lynne R. Wilkens1, Yurii B. Shvetsov1, Nicholas J. Ollberding2, Adrian A. Franke1, Brian E. Henderson3, Laurence N. Kolonel1, and Marc T. Goodman1 Abstract Background: Evidence from experimental and epidemiologic studies suggests that vitamin B6 may reduce the risk of breast cancer. Methods: We examined the association of prediagnostic plasma concentrations of pyridoxal-50-phosphate (PLP), an active form of vitamin B6, with postmenopausal breast cancer risk in a case–control study nested in the multiethnic cohort in Hawaii and Southern California, including 706 cases and 706 controls matched on date of birth, ethnicity, study site, date of blood draw, time of blood draw, hours of fasting before blood draw, and use of menopausal hormones. OR and 95% confidence intervals (CI) were calculated using conditional logistic regression models. Results: Women with plasma PLP concentrations in the highest quartile had a 30% reduced risk of invasive breast cancer (CI: 0.50–0.98) as compared with the women in the lowest PLP quartile (P for trend ¼ 0.02). The association seemed to be limited in cases with hormone receptor-positive tumors (P for heterogeneity ¼ 0.04); and remained unchanged in the analysis restricted to women with blood samples collected more than one year before cancer diagnosis (OR ¼ 0.69; CI: 0.48–0.99; P for trend ¼ 0.03). Conclusions: These data suggest that higher circulating levels of vitamin B6 are associated with a reduced risk of invasive postmenopausal breast cancer.
    [Show full text]
  • Summary Report
    Pyridoxal 5-Phosphate: Summary Report Item Type Report Authors Gianturco, Stephanie L.; Pavlech, Laura L.; Storm, Kathena D.; Yoon, SeJeong; Yuen, Melissa V.; Mattingly, Ashlee N. Publication Date 2019-12 Keywords Pyridoxal; Compounding; Food, Drug, and Cosmetic Act, Section 503B; Food and Drug Administration; Outsourcing facility; Drug compounding; Legislation, Drug; United States Food and Drug Administration; Pyridoxal Phosphate Rights Attribution-NoDerivatives 4.0 International Download date 02/10/2021 21:53:32 Item License http://creativecommons.org/licenses/by-nd/4.0/ Link to Item http://hdl.handle.net/10713/12348 Summary Report Pyridoxal 5-Phosphate Prepared for: Food and Drug Administration Clinical use of bulk drug substances nominated for inclusion on the 503B Bulks List Grant number: 2U01FD005946 Prepared by: University of Maryland Center of Excellence in Regulatory Science and Innovation (M-CERSI) University of Maryland School of Pharmacy December 2019 This report was supported by the Food and Drug Administration (FDA) of the U.S. Department of Health and Human Services (HHS) as part of a financial assistance award (U01FD005946) totaling $2,342,364, with 100 percent funded by the FDA/HHS. The contents are those of the authors and do not necessarily represent the official views of, nor an endorsement by, the FDA/HHS or the U.S. Government. 1 Table of Contents REVIEW OF NOMINATION ..................................................................................................... 4 METHODOLOGY ...................................................................................................................
    [Show full text]
  • Nutrition Journal of Parenteral and Enteral
    Journal of Parenteral and Enteral Nutrition http://pen.sagepub.com/ Micronutrient Supplementation in Adult Nutrition Therapy: Practical Considerations Krishnan Sriram and Vassyl A. Lonchyna JPEN J Parenter Enteral Nutr 2009 33: 548 originally published online 19 May 2009 DOI: 10.1177/0148607108328470 The online version of this article can be found at: http://pen.sagepub.com/content/33/5/548 Published by: http://www.sagepublications.com On behalf of: The American Society for Parenteral & Enteral Nutrition Additional services and information for Journal of Parenteral and Enteral Nutrition can be found at: Email Alerts: http://pen.sagepub.com/cgi/alerts Subscriptions: http://pen.sagepub.com/subscriptions Reprints: http://www.sagepub.com/journalsReprints.nav Permissions: http://www.sagepub.com/journalsPermissions.nav >> Version of Record - Aug 27, 2009 OnlineFirst Version of Record - May 19, 2009 What is This? Downloaded from pen.sagepub.com by Karrie Derenski on April 1, 2013 Review Journal of Parenteral and Enteral Nutrition Volume 33 Number 5 September/October 2009 548-562 Micronutrient Supplementation in © 2009 American Society for Parenteral and Enteral Nutrition 10.1177/0148607108328470 Adult Nutrition Therapy: http://jpen.sagepub.com hosted at Practical Considerations http://online.sagepub.com Krishnan Sriram, MD, FRCS(C) FACS1; and Vassyl A. Lonchyna, MD, FACS2 Financial disclosure: none declared. Preexisting micronutrient (vitamins and trace elements) defi- for selenium (Se) and zinc (Zn). In practice, a multivitamin ciencies are often present in hospitalized patients. Deficiencies preparation and a multiple trace element admixture (containing occur due to inadequate or inappropriate administration, Zn, Se, copper, chromium, and manganese) are added to par- increased or altered requirements, and increased losses, affect- enteral nutrition formulations.
    [Show full text]
  • BIOPAR DELTA-FORTE- 1 Nf Units, 50 Mcg Cbl, 2.5 Mg F-Thf, 1
    BIOPAR DELTA-FORTE- 1 nf units, 50 mcg cbl, 2.5 mg f-thf, 1 mg pteglu-, 7 mg me- thf capsule Jaymac Pharmacueticals LLC Disclaimer: This drug has not been found by FDA to be safe and effective, and this labeling has not been approved by FDA. For further information about unapproved drugs, click here. ---------- BioparTM delta-FORTE DESCRIPTION [1 NF Units] [50 mcg CBl] [2.5 mg F-THf] [1 mg PteGlu-] [7 mg Me-THf] Prescription Hematopoietic Preparation For Therapeutic Use Multiphasic Softgels (30ct carton) NDC 64661-793-30 Rx ONLY BioparTMdelta-FORTE is an orally administered prescription hematopoietic preparation for therapeutic use formulated for adult macrocytic anemia patients – specifically including pernicious anemia patients, ages 12 and up, who are under specific direction and monitoring of cobalamin and folate status by a physician. A recent study+ suggested that BioparTM delta-FORTE was effective in lowering homocysteine levels in patients that are positive for MTHFR (methylenetetrahydrofolate reductase polymorphism). BioparTM delta-FORTE may be taken by women of childbearing age. BioparTM delta- FORTE may be taken by geriatric patients where compliance is an issue. + ClinicalTrials.gov identifier: NCT02709668, Correlation of Clinical Response With Homocysteine Reduction During Therapy With Reduced B Vitamins in Patients with MDD Who Are Positive for MTHFR C677T or A1298C Polymorphism. INGREDIENTS Cobalamin-intrinsic factor concentrate (non-inhibitory)1 .............................................................................................
    [Show full text]
  • A Simplified Method for Determination of Pyridoxal Phosphate in Biological Samples
    Upsala J Med Sci 91: 105-109, 1986 A Simplified Method for Determination of Pyridoxal Phosphate in Biological Samples Arne Hamfelt Department of Clinical Chemistry, Central Hospital Sundsvall, Sundsvall, Sweden ABSTRACT A new method for the determination of pyridoxal phosphate in plasma and in cerebrospinal fluid is described. It is based on the generally accepted apotyrosine decarboxylase method, but, in stead of following the decarboxylation rate using I4C- och 7 H-labelled tyrosine, a high performance liquid chromatography (HPLC) method for separation of tyrosine and tyramine is used. This procedure is recommended as it is less time consuming and avoids utilizing radioactive material. INTRODUCTION The level of pyridoxal phosphate in plasma and in cerebrospinal fluid lies in lower nanomolar range per liter, hence sensitive assay procedures must be utilized. These have most often been based on using pyridoxal phosphate as coenzyme in a pyridoxal phosphate dependent enzymatic reaction. The apoenzyme has been prepared and the conversion of the substrate traced. By adding varying amounts of pyridoxal phosphate the rate of enzymatic reaction has been calculated and a calibration curve obtained. The enzyme used has often been tyrosine decarboxylase, the apoenzyme of which is rather easily prepared. The first description of this enzyme reaction for this purpose was by Boxer and al. in 1957 (2), who followed the reaction rate by measuring the carbon dioxide produced in a Warburg equipment. The method was made more sensitive by using tyr~sine-l-’~C (3), later changed to a mixture of tyr~sine-l-’~Cand 3H-tyrosine, determining the I4C and 7 H activity at different time intervals in a dual channel liquid scintillation counter.
    [Show full text]
  • Comparison of Dietary Vitamin B6 and Niacin on Fattenning Performance of Quails
    Comparison of dietary vitamin b6 and niacin on fattenning performance of quails C. GUL¹* and O. OZTURKCAN²** ¹ /Vocational School of Yildizeli , Cumhuriyet University, Sivas-TURKEY. *e-mail: [email protected] ² Deparment of Animal Science, Faculty of Agriculture, Cukurova University, Adana- TURKEY. **e-mail: [email protected] The present study was conducted to determine whether dietary vitamin B6 and niacin could increase weight gain and reduce fat content of japanese quail (Coturnix coturnix japonica) two experiments were carried out during the experimental study. The first experiment was performed using 60 japanese quails age of 5 weeks. The chicks were divided into 4 groups of equal number and fed experimental diets supplemented with 0, 2.53, 2.76 or 3.22 mg/kg vitamin B6. At the end of the experiment, feed consumption, feed efficiency, carcass weight, carcass yield and abdominal fat weight were not significantly improved by B6 supplementation (P>0.05). In the second experiment, sixty 1-day-old japanese quails were divided into 4 groups, comprising 15 birds each and fed experimental diets supplemented with 0, 44, 48 or 56 mg/kg niacin. Dietary niacin levels did not affect body weight, body weight gain, feed consumption, feed efficiency, abdominal fat deposition and carcass weight (P>0.05). The result of this study demonstrated that chicks receiving vitamin B6 and niacin supplementation did not affect performance, abdominal fat deposition and carcass weight. Key Words: Japanese Quail; Niacin; Vitamin B6; Abdominal Fat Introduction Quails and poultry have similar nutrition physiology. Due to their metabolism rate, feed intake and energy requirements are high (Zucker and Groop, 1967).
    [Show full text]
  • Effects of Vitamin B6 Metabolism on Oncogenesis, Tumor Progression and Therapeutic Responses
    Oncogene (2013) 32, 4995–5004 & 2013 Macmillan Publishers Limited All rights reserved 0950-9232/13 www.nature.com/onc REVIEW Effects of vitamin B6 metabolism on oncogenesis, tumor progression and therapeutic responses L Galluzzi1,2,8, E Vacchelli2,3,4, J Michels2,3,4, P Garcia2,3,4, O Kepp2,3,4, L Senovilla2,3,4, I Vitale2,3,4 and G Kroemer1,4,5,6,7,8 Pyridoxal-50-phosphate (PLP), the bioactive form of vitamin B6, reportedly functions as a prosthetic group for 44% of classified enzymatic activities of the cell. It is therefore not surprising that alterations of vitamin B6 metabolism have been associated with multiple human diseases. As a striking example, mutations in the gene coding for antiquitin, an evolutionary old aldehyde dehydrogenase, result in pyridoxine-dependent seizures, owing to the accumulation of a metabolic intermediate that inactivates PLP. In addition, PLP is required for the catabolism of homocysteine by transsulfuration. Hence, reduced circulating levels of B6 vitamers (including PLP as well as its major precursor pyridoxine) are frequently paralleled by hyperhomocysteinemia, a condition that has been associated with an increased risk for multiple cardiovascular diseases. During the past 30 years, an intense wave of clinical investigation has attempted to dissect the putative links between vitamin B6 and cancer. Thus, high circulating levels of vitamin B6, as such or as they reflected reduced amounts of circulating homocysteine, have been associated with improved disease outcome in patients bearing a wide range of hematological and solid neoplasms. More recently, the proficiency of vitamin B6 metabolism has been shown to modulate the adaptive response of tumor cells to a plethora of physical and chemical stress conditions.
    [Show full text]